ID G4RPL8_THETK Unreviewed; 981 AA.
AC G4RPL8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN Name=ileS {ECO:0000313|EMBL:CCC81513.1};
GN OrderedLocusNames=TTX_0858 {ECO:0000313|EMBL:CCC81513.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81513.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC81513.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000114};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363035}.
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DR EMBL; FN869859; CCC81513.1; -; Genomic_DNA.
DR RefSeq; WP_014126769.1; NC_016070.1.
DR AlphaFoldDB; G4RPL8; -.
DR STRING; 768679.TTX_0858; -.
DR PaxDb; 768679-TTX_0858; -.
DR GeneID; 11261753; -.
DR KEGG; ttn:TTX_0858; -.
DR PATRIC; fig|768679.9.peg.867; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OrthoDB; 30823at2157; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT DOMAIN 17..639
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 688..837
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 981 AA; 114999 MW; 9A4FB8BF7D334956 CRC64;
MTPSAYDPLK IEEEVRAFWD EREIPKKWRA FDQKAERRFT FLEGPPTTNG FPHVGHIRGR
TYKDVVLRFW RSRGFSVWAQ GGWDMQGLPV ELEVEQRQGL KSKKDIEKFG VDKFVQECNK
LDDYYLQFWE EWGTKRLGLW LDLENAYQTR KPQYIEYAWR LLKRAHEKGL LAEDYRVLWF
CPRCETSLSD HEVDLGYAER EDPSIYVKFR VEGEEDEYLV IWTTTPWTIV DNEAVAVAPD
VAYAKVEVSW EGRRERWWMA EKLVPQLMQM FGIREWRVLE IKNGKELAGL RYIHPLAEEV
PERATRQHQV YPADFVTLEQ GTGLVHVAPG HGPEDFELAL KYGIRVTNSV EINGIYNQLG
GKYAGMYVFD VDKKVIEDLK AKGLLVYKSS IRHEYPHCWR CGTKLILRAD RQWFIRISVL
RERMYDELKK VKIYPEKLRY RFDDFVRNAR DWNISRSRFW GTPLPIWRCK KDGRILVIGS
IEELKRLAKE LPPVDDFWLV HRPWIDQVKL STPDCDEWIR EPYVADVWMD SGIAWIAAVD
GERNPELWSA LYPFSWVTEA IDQTRGWFYS LLATSMVYLG RAPYKSILIS GHILDKQGQK
MSKSKGNVVW AKDLLSKYGA DPTRLYLLTK AAPWEALNFD PDEIKYALSQ LNILWNVVKF
ADTYMQLDGF NAQKHTLPTM IHKALDEDRW LLSETNLLIQ RVAKHMENFE IHEAAKAWVD
FIVETLSHRY IRLLRRRVWT EEPREDKYAA YAVLFHALRS ALIIGGIFVP HVAEYLWQHF
IRKYDQNAAE SVHLAQYPEP GEVDEELVKS FDELFTVFSI AAEARNKAGI KLRWPISRLI
VKGAQMALKH ADLLAYLANA KVVEEGECSA DWIVHEERGI TVCIPRKLDS ELFYEALARE
LVRRVQVMRK EAGLSIEDFI ELYIETEAQD LRDAVKHFGQ YIANEVRATR LELGVGPSGL
YSREWTIEDM RVKIYLKKAT R
//
